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PDBsum entry 4gbk

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protein ligands metals Protein-protein interface(s) links
Hormone PDB id
4gbk
Jmol
Contents
Protein chains
21 a.a.
29 a.a.
30 a.a.
Ligands
CRS ×2
Metals
_CL ×2
_ZN ×2
PDB id:
4gbk
Name: Hormone
Title: Crystal structure of aspart insulin at ph 8.5
Structure: Insulin a chain. Chain: a, c. Fragment: unp residues 90-110. Insulin b chain. Chain: b, d. Fragment: unp residues 25-54. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Resolution:
2.40Å     R-factor:   0.201     R-free:   0.266
Authors: L.M.T.R.Lima,M.P.Favero-Retto,L.C.Palmieri
Key ref: L.C.Palmieri et al. (2013). A T3R3 hexamer of the human insulin variant B28Asp. Biophys Chem, 173, 1-7. PubMed id: 23428413 DOI: 10.1016/j.bpc.2013.01.003
Date:
27-Jul-12     Release date:   12-Jun-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
21 a.a.
Protein chain
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
29 a.a.*
Protein chain
Pfam   ArchSchema ?
P01308  (INS_HUMAN) -  Insulin
Seq:
Struc:
110 a.a.
30 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     hormone activity     1 term  

 

 
DOI no: 10.1016/j.bpc.2013.01.003 Biophys Chem 173:1-7 (2013)
PubMed id: 23428413  
 
 
A T3R3 hexamer of the human insulin variant B28Asp.
L.C.Palmieri, M.P.Fávero-Retto, D.Lourenço, L.M.Lima.
 
  ABSTRACT  
 
Insulin shows a complex equilibrium between monomers and hexamers, involving varying conformers and association states. We sought to perform a structural characterization of the fast-acting human insulin variant B28Asp ("aspart"). Small-angle X-ray scattering measurements reveal similar globular behavior in both the aspart and regular human insulin, with a Rg of 19Å and a Dmax of approximately 50Å, indicating similar mean quaternary assembly distribution. Crystallographic assays revealed a T3R3 assembly of the aspart insulin formed by the TR dimer in the asymmetric unit, with all the first 8 residues of the B chain in the R-state monomer in helical conformation and the participation of its B3Asn in the stabilization of the hexamer. Our data provide access to novel structural information on aspart insulin such as an aspart insulin dimer in solution, the aspart insulin in T conformation and a pure R-state conformer establishing a T3R3 assembly, providing further insight on the stepwise conformational transition and assembly of this fast-insulin.